Steinhagen-Thiessen E, Hilz H
Mech Ageing Dev. 1976;5(6):447-57. doi: 10.1016/0047-6374(76)90043-9.
In human striated muscle obtained in surgery, an age-dependent decrease in aldolase and creatine kinase specific activities and an increase in DNA content per wet weight was found. In the group of the elderly (64-84 years), the enzymes decreased by 40-60% when compared with a group between 24 and 47 years old, while DNA content rose by a factor of 1.53 indicating loss of tissue water. Titration of aldolase and creatine kinase molecules by specific antibodies against aldolase A and creatine kinase MM isozymes, respectively, revealed very little accumulation of aldolase cross-reacting materials in the old age group (1.13 fold), and no accumulation of inactive creatine kinase molecules. Similar conclusions can be drawn from thermostability analyses of these two enzymes. The data do not support the view that accumulation of modified proteins due to random errors or to post-translational alternations is a general or causative phenomenon of aging in human muscle tissue.
在手术中获取的人体横纹肌中，发现醛缩酶和肌酸激酶的比活性随年龄增长而降低，每湿重的DNA含量增加。在老年人组（64 - 84岁）中，与24至47岁的组相比，这些酶降低了40 - 60%，而DNA含量增加了1.53倍，表明组织水分流失。分别用抗醛缩酶A和肌酸激酶MM同工酶的特异性抗体滴定醛缩酶和肌酸激酶分子，结果显示老年组中醛缩酶交叉反应物质的积累很少（1.13倍），且无无活性肌酸激酶分子的积累。从这两种酶的热稳定性分析中也可得出类似结论。这些数据不支持以下观点：由于随机误差或翻译后修饰导致的修饰蛋白积累是人类肌肉组织衰老的普遍或致病现象。
